Detection of Human Phospho-DDR2 (Y740) by Simple WesternTM.
Simple Western lane view shows lysates of HEK293 human embryonic kidney cell line transfected with human DDR2 untreated (-) or treated (+) with Calyculin A for 10 minutes, loaded at 0.2 mg/mL. A specific band was detected for Phospho-DDR2 (Y740) at approximately 130 kDa (as indicated) using 1:100 dilution of Rabbit Anti-Human Phospho-DDR2 (Y740) Monoclonal Antibody (Catalog # MAB25382). This experiment was conducted under reducing conditions and using the66-440 kDa separation system.

Preparation and Storage

Shipping

The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below. *Small pack size (SP) is shipped with polar packs. Upon receipt, store it immediately at -20 to -70 °C

Stability & Storage

Use a manual defrost freezer and avoid repeated freeze-thaw cycles.

12 months from date of receipt, -20 to -70 °C, as supplied.

1 month, 2 to 8 °C under sterile conditions after opening.

6 months, -20 to -70 °C under sterile conditions after opening.

Background: DDR2

DDR2, also known as TYR010 and TKT, is a widely expressed 130 kDa type I transmembrane glycoprotein belonging to the discoidin-like domain containing subfamily of receptor tyrosine kinases (1). Mature human DDR2 consists of a 378 amino acid (aa) extracellular domain (ECD) that includes the discoidin-like domain, a 22 aa transmembrane segment, and a 434 aa cytoplasmic domain that includes the kinase domain (2). Within the ECD, human DDR2 shares 53% aa sequence identity with DDR1 and 97% aa sequence identity with mouse DDR2. The discoidin-like domain mediates DDR2 interactions with collagens I, III, and X (3-5). Collagens II and V are less efficacious ligands (3). DDR2 selectively recognizes the triple helical structure of collagen compared to monomeric or denatured collagen (3, 5, 6). Within collagen II, the D2 period is required for DDR2 binding, and the D1 period is additionally required to trigger DDR2 autophosphorylation (6). The ECD of DDR2 exists as a non-covalent dimer in solution, and dimerization of the receptor greatly enhances collagen binding (4, 7). DDR2 interaction with collagen I inhibits collagen fibrillogenesis and alters collagen fiber morphology (7). Ligand binding induces DDR2 autophosphorylation in the cytoplasmic domain (3, 5, 8), which promotes associations with Shc and Src (9). In addition to the above mechanism, DDR2 exhibits a distinct interaction with collagen X. A region other than the discoidin-like domain of DDR2 recognizes the non-helical NC1 domain of collagen X, and this interaction does not lead to receptor autophosphorylation (5). Activation of DDR2 by collagen induces upregulation of MMP-1, -2, and -13 as well as DDR2 itself (3, 8, 10). DDR2 is implicated in collagenous matrix destruction and cell invasiveness (8, 10). DDR2 is also upregulated in several pathological conditions, including hepatic fibrosis following injury, rheumatoid and osteoarthritis, and smooth muscle cell hyperplasia (8, 10-12).

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The data collected includes not only links to publications in PubMed,
but also provides information about sample types, species, and experimental conditions.

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